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Mutant glycosyltransferases assist in the development of a targeted drug delivery system and contrast agents for MRI

  1. Author:
    Qasba, P. K.
    Ramakrishnan, B.
    Boeggeman, E.

  2. Author Address

    CCRNP, Struct Glycobiol Sect, NCI Frederick, Nanobiol Program, Frederick, MD 21702 USA. SAIC Frederick Inc, Basic Res Program, Frederick, MD USA.;Qasba, PK, CCRNP, Struct Glycobiol Sect, NCI Frederick, Nanobiol Program, Bldg 469,Room 221, Frederick, MD 21702 USA.;qasba@helix.nih.gov
    1. Year: 2006
  2. Journal: Aaps Journal
    1. 8
    2. 1
    3. Pages: E190-E195
  4. Type of Article: Review
  5. ISSN: 1550-7416
  1. Abstract:

    The availability of structural information on glycosyltransferases is beginning to make structure-based reengineering of these enzymes possible. Mutant glycosyltransferases have been generated that can transfer a sugar residue with a chemically reactive unique functional group to a sugar moiety of glycoproteins, glycolipids, and proteoglycans (glycoconjugates). The presence of modified sugar moiety on a glycoprotein makes it possible to link bioactive molecules via modified glycan chains, thereby assisting in the assembly of bionanoparticles that are useful for developing the targeted drug delivery system and contrast agents for magnetic resonance imaging. The reengineered recombinant glycosyltransferases also make it possible to (1) remodel the oligosaccharide chains of glycoprotein drugs, and (2) synthesize oligosaccharides for vaccine development.

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External Sources

  1. View record in Web of Science®
  2. WOS: 000236804800023

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